Toxoplasma gondii Clp family protein: TgClpB1 plays a crucial role in thermotolerance

文献类型： 外文期刊

第一作者： Cao, Shinuo

作者： Cao, Shinuo;Du, Nali;Chen, Heming;Pang, Yu;Zhang, Zhaoxia;Zheng, Jun;Jia, Honglin

作者机构：

关键词： ClpB;caseinolytic proteases and chaperones;AAA plus ATPases;thermotolerance;toxoplasma gondii

期刊名称：ONCOTARGET （ 影响因子：5.168； 五年影响因子：5.312 ）

ISSN： 1949-2553

年卷期： 2017 年 8 卷 49 期

页码：

收录情况： SCI

摘要： Caseinolytic peptidase B (ClpB) plays a pivotal role in suppressing and reversing protein aggregation. Toxoplasma gondii is an intracellular parasitic protozoan that infects a wide variety of mammals and birds and therefore is exposed to a broad range of living condition. We screened ToxoDB (http://ToxoDB.org) and identified 10 putative T. gondii genes encoding members of the Clp superfamily of caseinolytic proteases and chaperones. Of these, we focused on characterizing the Class I ATP-dependent molecular chaperones TgClpB1, TgClpB2, and TgClpB3. We found that TgClpB1, the most divergent of the five T. gondii Class I Clp ATPases, is cytoplasmic, TgClpB2 is found in the mitochondria of the parasites, and TgClpB3 is a ClpB with novel apicoplast localization. Knockout strains of TgClpB1 and TgClpB2 were established by CRISPR/Cas9 mutagenesis, and their complementing strains were constructed with FLAG-tag. Although knockout of TgClpB1 or TgClpB2 did not affect growth under normal circumstances, TgClpB1 was required for T. gondii thermotolerance. The growth, replication, and invasion capabilities of TgClpB1-deficient mutants were significantly inhibited after extracellular parasites were pretreated at 45 degrees C. Moreover, TgClpB1 were observed at the poles of the Delta TgClpB1 FLAG-tagged strain treated at 42 degrees C.

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